HIS4/YCL030C Summary Help

Standard Name HIS4 1, 2
Systematic Name YCL030C
Feature Type ORF, Verified
Description Multifunctional enzyme containing phosphoribosyl-ATP pyrophosphatase; phosphoribosyl-AMP cyclohydrolase, and histidinol dehydrogenase activities; catalyzes the second, third, ninth and tenth steps in histidine biosynthesis (3 and see Summary Paragraph)
Name Description HIStidine requiring 2
Chromosomal Location
ChrIII:68333 to 65934 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: -22 cM
Gene Ontology Annotations All HIS4 GO evidence and references
  View Computational GO annotations for HIS4
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 16 genes
Resources
Pathways
Classical genetics
unspecified
Large-scale survey
null
Resources
30 total interaction(s) for 25 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 17
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 1
  • Biochemical Activity: 1

Genetic Interactions
  • Dosage Rescue: 1
  • Phenotypic Suppression: 3
  • Positive Genetic: 1
  • Synthetic Growth Defect: 1
  • Synthetic Rescue: 4

Resources
Expression Summary
histogram
Resources
Length (a.a.) 799
Molecular Weight (Da) 87,721
Isoelectric Point (pI) 5.04
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIII:68333 to 65934 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: -22 cM
Last Update Coordinates: 2000-09-13 | Sequence: 2000-09-13
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2400 68333..65934 2000-09-13 2000-09-13
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000535
SUMMARY PARAGRAPH for HIS4

HIS4 encodes a multifunctional polypeptide that has phosphoribosyl-ATP pyrophosphatase, phosphoribosyl-AMP cyclohydrolase, and histidinol dehydrogenase activities. Phosphoribosyl-ATP pyrophosphatase and phosphoribosyl-AMP cyclohydrolase catalyze the second and third steps in histidine biosynthesis, respectively, and histidinol dehydrogenase catalyzes the last two steps (4). The biosynthesis of histidine has been most extensively studied in Salmonella typhimurium and E. coli. The reactions and enzymes involved in histidine biosynthesis have been identified in many organisms, and are thoroughly reviewed in Alifano et al. (4). Mutations in HIS4, as well as in genes encoding other histidine biosynthetic enzymes, cause histidine auxotrophy and sensitivity to copper, cobalt, and nickel salts (5). Transcription of HIS4 is regulated by general amino acid control, in which the transcription factor Gcn4p plays a key role (reviewed in 6). The transcription factors Bas1p and Bas2p also activate HIS4 transcription (7). Because it is near a recombination hotspot, HIS4 has been widely used in studies of recombination (for example, see 8 and 9).

Last updated: 1999-11-12 Contact SGD

References cited on this page View Complete Literature Guide for HIS4
1) Donahue TF, et al.  (1982) The nucleotide sequence of the HIS4 region of yeast. Gene 18(1):47-59
2) Shaffer B, et al.  (1969) Nonsense mutations affecting the his4 enzyme complex of yeast. Proc Natl Acad Sci U S A 63(4):1198-205
3) Keesey JK Jr, et al.  (1979) The product of the his4 gene cluster in Saccharomyces cerevisiae. A trifunctional polypeptide. J Biol Chem 254(15):7427-33
4) Alifano P, et al.  (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69
5) Pearce DA and Sherman F  (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9
6) Hinnebusch A  (1992) "General and Pathway-specific Regulatory Mechanisms Controlling the Synthesis of Amino Acid Biosynthetic Enzymes in Saccharomyces cerevisiae". Pp. 319-414 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
7) Denis V, et al.  (1998) Role of the myb-like protein bas1p in Saccharomyces cerevisiae: a proteome analysis. Mol Microbiol 30(3):557-66
8) Foss HM, et al.  (1999) The conversion gradient at HIS4 of Saccharomyces cerevisiae. II. A role for mismatch repair directed by biased resolution of the recombinational intermediate. Genetics 153(2):573-83
9) Kirkpatrick DT, et al.  (1999) Maximal stimulation of meiotic recombination by a yeast transcription factor requires the transcription activation domain and a DNA-binding domain. Genetics 152(1):101-15